Fig. 1.

(A and B) Experimental (A) SAXS in 100% H₂O and (B) SANS in 100% D₂O profiles are shown in black squares and circles, respectively. Experimental Kratky plots, I(q) × q² vs. q shown in the Insets confirm the unfolded structure of SH4UD. The ensemble-averaged profiles calculated from ∼510-ns HREMD trajectory are shown as a red line. (C) Comparison between experimental and calculated (HREMD) NMR chemical shifts, expressed in parts per million (ppm), of the backbone N^H, C^α, and C^β atoms. The NMR experimental data are taken from Biological Magnetic Resonance Data Bank entry 15563 (12) and the theoretical chemical shifts were calculated using SHIFTX2 from ∼51,000 structures (122). (D) Radius of gyration $\left(R_g^N\right)$ of a protein segment consisting of N residues calculated from the HREMD simulation. The red line is a fit of Eq. 1 to the data.